Regulation of Pyruvate Kinase Type M2 by A-Raf: A Possible Glycolytic Stop or Go Mechanism
Recently a link between A-Raf, cellular energy homeostasis and synthetic pathways has been suggested through the identification of pyruvate kinase type M2 (M2-PK), a key glycolytic enzyme, as interaction partner of A-Raf. In this study, we demonstrated that A-Raf is an important regulator of M2-PK f...
Gespeichert in:
| Veröffentlicht in: | Anticancer research 2007-11, Vol.27 (6B), p.3963-3971 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 3971 |
|---|---|
| container_issue | 6B |
| container_start_page | 3963 |
| container_title | Anticancer research |
| container_volume | 27 |
| creator | MAZUREK, Sybille DREXLER, Hannes C. A TROPPMAIR, Jakob EIGENBRODT, Erich RAPP, Ulf R |
| description | Recently a link between A-Raf, cellular energy homeostasis and synthetic pathways has been suggested through the identification
of pyruvate kinase type M2 (M2-PK), a key glycolytic enzyme, as interaction partner of A-Raf. In this study, we demonstrated
that A-Raf is an important regulator of M2-PK function. In primary mouse fibroblasts, which are characterized by glutamine
production and serine degradation, A-Raf induced dimerization and inactivation of M2-PK, thereby reducing conversion rates
from glucose to lactate. In immortalized NIH3T3 fibroblasts, showing glutamine degradation and serine production, oncogenic
A-Raf increased the highly active tetrameric form of M2-PK and favored glycolytic energy production. High serine levels thus
may be responsible for the activation of M2-PK in A-Raf transformed NIH3T3 cells. |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_70083325</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>70083325</sourcerecordid><originalsourceid>FETCH-LOGICAL-h301t-c2089fe3b624870a6a7eee09ce0e5a1414a4c01d94a5b49dc26c55aff187b9773</originalsourceid><addsrcrecordid>eNqF0DtPwzAUBeAIgaA8_gLyAlskP2I7ZisVFAQVCMrCEt24N62RE5c4AeXfU4ki2JjO8uno6OwkI6YNS7UUdDcZUS5pqimVB8lhjG-UKmVysZ8csJxzKaUeJa9PuOw9dC40JFTkcWj7D-iQ3LkGIpL5sEYy46QcyDh9guqCjMljiNGVHsnUDzb4oXOWPHdhTUJLpoHM0K6gcbE-TvYq8BFPtnmUvFxfzSc36f3D9HYyvk9XgrIutZzmpkJRKp7lmoICjYjUWKQogWUsg8xStjAZyDIzC8uVlRKqiuW6NFqLo-T8u3fdhvceY1fULlr0HhoMfSw2B-RCcPkv5FQxxTTdwNMt7MsaF8W6dTW0Q_Fz2wacbQFEC75qobEu_jpjMpOJP9NWbrn6dC0WsQbvN7WigJbrQl0WwighvgB_TIIg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>20616170</pqid></control><display><type>article</type><title>Regulation of Pyruvate Kinase Type M2 by A-Raf: A Possible Glycolytic Stop or Go Mechanism</title><source>MEDLINE</source><source>EZB Electronic Journals Library</source><creator>MAZUREK, Sybille ; DREXLER, Hannes C. A ; TROPPMAIR, Jakob ; EIGENBRODT, Erich ; RAPP, Ulf R</creator><creatorcontrib>MAZUREK, Sybille ; DREXLER, Hannes C. A ; TROPPMAIR, Jakob ; EIGENBRODT, Erich ; RAPP, Ulf R</creatorcontrib><description>Recently a link between A-Raf, cellular energy homeostasis and synthetic pathways has been suggested through the identification
of pyruvate kinase type M2 (M2-PK), a key glycolytic enzyme, as interaction partner of A-Raf. In this study, we demonstrated
that A-Raf is an important regulator of M2-PK function. In primary mouse fibroblasts, which are characterized by glutamine
production and serine degradation, A-Raf induced dimerization and inactivation of M2-PK, thereby reducing conversion rates
from glucose to lactate. In immortalized NIH3T3 fibroblasts, showing glutamine degradation and serine production, oncogenic
A-Raf increased the highly active tetrameric form of M2-PK and favored glycolytic energy production. High serine levels thus
may be responsible for the activation of M2-PK in A-Raf transformed NIH3T3 cells.</description><identifier>ISSN: 0250-7005</identifier><identifier>EISSN: 1791-7530</identifier><identifier>PMID: 18225557</identifier><language>eng</language><publisher>Attiki: International Institute of Anticancer Research</publisher><subject>Animals ; Biological and medical sciences ; Cell Transformation, Neoplastic - metabolism ; Dimerization ; Fibroblasts - enzymology ; Fibroblasts - pathology ; Glutamine - metabolism ; Glycolysis ; HT29 Cells ; Humans ; Immunoprecipitation ; Medical sciences ; Mice ; NIH 3T3 Cells ; Proto-Oncogene Proteins A-raf - metabolism ; Pyruvate Kinase - metabolism ; Serine - metabolism ; Tumors</subject><ispartof>Anticancer research, 2007-11, Vol.27 (6B), p.3963-3971</ispartof><rights>2008 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19949437$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18225557$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MAZUREK, Sybille</creatorcontrib><creatorcontrib>DREXLER, Hannes C. A</creatorcontrib><creatorcontrib>TROPPMAIR, Jakob</creatorcontrib><creatorcontrib>EIGENBRODT, Erich</creatorcontrib><creatorcontrib>RAPP, Ulf R</creatorcontrib><title>Regulation of Pyruvate Kinase Type M2 by A-Raf: A Possible Glycolytic Stop or Go Mechanism</title><title>Anticancer research</title><addtitle>Anticancer Res</addtitle><description>Recently a link between A-Raf, cellular energy homeostasis and synthetic pathways has been suggested through the identification
of pyruvate kinase type M2 (M2-PK), a key glycolytic enzyme, as interaction partner of A-Raf. In this study, we demonstrated
that A-Raf is an important regulator of M2-PK function. In primary mouse fibroblasts, which are characterized by glutamine
production and serine degradation, A-Raf induced dimerization and inactivation of M2-PK, thereby reducing conversion rates
from glucose to lactate. In immortalized NIH3T3 fibroblasts, showing glutamine degradation and serine production, oncogenic
A-Raf increased the highly active tetrameric form of M2-PK and favored glycolytic energy production. High serine levels thus
may be responsible for the activation of M2-PK in A-Raf transformed NIH3T3 cells.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell Transformation, Neoplastic - metabolism</subject><subject>Dimerization</subject><subject>Fibroblasts - enzymology</subject><subject>Fibroblasts - pathology</subject><subject>Glutamine - metabolism</subject><subject>Glycolysis</subject><subject>HT29 Cells</subject><subject>Humans</subject><subject>Immunoprecipitation</subject><subject>Medical sciences</subject><subject>Mice</subject><subject>NIH 3T3 Cells</subject><subject>Proto-Oncogene Proteins A-raf - metabolism</subject><subject>Pyruvate Kinase - metabolism</subject><subject>Serine - metabolism</subject><subject>Tumors</subject><issn>0250-7005</issn><issn>1791-7530</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0DtPwzAUBeAIgaA8_gLyAlskP2I7ZisVFAQVCMrCEt24N62RE5c4AeXfU4ki2JjO8uno6OwkI6YNS7UUdDcZUS5pqimVB8lhjG-UKmVysZ8csJxzKaUeJa9PuOw9dC40JFTkcWj7D-iQ3LkGIpL5sEYy46QcyDh9guqCjMljiNGVHsnUDzb4oXOWPHdhTUJLpoHM0K6gcbE-TvYq8BFPtnmUvFxfzSc36f3D9HYyvk9XgrIutZzmpkJRKp7lmoICjYjUWKQogWUsg8xStjAZyDIzC8uVlRKqiuW6NFqLo-T8u3fdhvceY1fULlr0HhoMfSw2B-RCcPkv5FQxxTTdwNMt7MsaF8W6dTW0Q_Fz2wacbQFEC75qobEu_jpjMpOJP9NWbrn6dC0WsQbvN7WigJbrQl0WwighvgB_TIIg</recordid><startdate>20071101</startdate><enddate>20071101</enddate><creator>MAZUREK, Sybille</creator><creator>DREXLER, Hannes C. A</creator><creator>TROPPMAIR, Jakob</creator><creator>EIGENBRODT, Erich</creator><creator>RAPP, Ulf R</creator><general>International Institute of Anticancer Research</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7TO</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20071101</creationdate><title>Regulation of Pyruvate Kinase Type M2 by A-Raf: A Possible Glycolytic Stop or Go Mechanism</title><author>MAZUREK, Sybille ; DREXLER, Hannes C. A ; TROPPMAIR, Jakob ; EIGENBRODT, Erich ; RAPP, Ulf R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h301t-c2089fe3b624870a6a7eee09ce0e5a1414a4c01d94a5b49dc26c55aff187b9773</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cell Transformation, Neoplastic - metabolism</topic><topic>Dimerization</topic><topic>Fibroblasts - enzymology</topic><topic>Fibroblasts - pathology</topic><topic>Glutamine - metabolism</topic><topic>Glycolysis</topic><topic>HT29 Cells</topic><topic>Humans</topic><topic>Immunoprecipitation</topic><topic>Medical sciences</topic><topic>Mice</topic><topic>NIH 3T3 Cells</topic><topic>Proto-Oncogene Proteins A-raf - metabolism</topic><topic>Pyruvate Kinase - metabolism</topic><topic>Serine - metabolism</topic><topic>Tumors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MAZUREK, Sybille</creatorcontrib><creatorcontrib>DREXLER, Hannes C. A</creatorcontrib><creatorcontrib>TROPPMAIR, Jakob</creatorcontrib><creatorcontrib>EIGENBRODT, Erich</creatorcontrib><creatorcontrib>RAPP, Ulf R</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Anticancer research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MAZUREK, Sybille</au><au>DREXLER, Hannes C. A</au><au>TROPPMAIR, Jakob</au><au>EIGENBRODT, Erich</au><au>RAPP, Ulf R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of Pyruvate Kinase Type M2 by A-Raf: A Possible Glycolytic Stop or Go Mechanism</atitle><jtitle>Anticancer research</jtitle><addtitle>Anticancer Res</addtitle><date>2007-11-01</date><risdate>2007</risdate><volume>27</volume><issue>6B</issue><spage>3963</spage><epage>3971</epage><pages>3963-3971</pages><issn>0250-7005</issn><eissn>1791-7530</eissn><abstract>Recently a link between A-Raf, cellular energy homeostasis and synthetic pathways has been suggested through the identification
of pyruvate kinase type M2 (M2-PK), a key glycolytic enzyme, as interaction partner of A-Raf. In this study, we demonstrated
that A-Raf is an important regulator of M2-PK function. In primary mouse fibroblasts, which are characterized by glutamine
production and serine degradation, A-Raf induced dimerization and inactivation of M2-PK, thereby reducing conversion rates
from glucose to lactate. In immortalized NIH3T3 fibroblasts, showing glutamine degradation and serine production, oncogenic
A-Raf increased the highly active tetrameric form of M2-PK and favored glycolytic energy production. High serine levels thus
may be responsible for the activation of M2-PK in A-Raf transformed NIH3T3 cells.</abstract><cop>Attiki</cop><pub>International Institute of Anticancer Research</pub><pmid>18225557</pmid><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0250-7005 |
| ispartof | Anticancer research, 2007-11, Vol.27 (6B), p.3963-3971 |
| issn | 0250-7005 1791-7530 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_70083325 |
| source | MEDLINE; EZB Electronic Journals Library |
| subjects | Animals Biological and medical sciences Cell Transformation, Neoplastic - metabolism Dimerization Fibroblasts - enzymology Fibroblasts - pathology Glutamine - metabolism Glycolysis HT29 Cells Humans Immunoprecipitation Medical sciences Mice NIH 3T3 Cells Proto-Oncogene Proteins A-raf - metabolism Pyruvate Kinase - metabolism Serine - metabolism Tumors |
| title | Regulation of Pyruvate Kinase Type M2 by A-Raf: A Possible Glycolytic Stop or Go Mechanism |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-29T07%3A45%3A32IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Regulation%20of%20Pyruvate%20Kinase%20Type%20M2%20by%20A-Raf:%20A%20Possible%20Glycolytic%20Stop%20or%20Go%20Mechanism&rft.jtitle=Anticancer%20research&rft.au=MAZUREK,%20Sybille&rft.date=2007-11-01&rft.volume=27&rft.issue=6B&rft.spage=3963&rft.epage=3971&rft.pages=3963-3971&rft.issn=0250-7005&rft.eissn=1791-7530&rft_id=info:doi/&rft_dat=%3Cproquest_pubme%3E70083325%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=20616170&rft_id=info:pmid/18225557&rfr_iscdi=true |